Reviewed, UniProtKB/Swiss-Prot Q55C91 (ALN2_DICDI)

Names and origin

Protein names

Recommended name:
    Probable allantoinase 2
    EC=3.5.2.5

Gene names

Name:	allB2
ORF Names:	DDB_G0270162

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	(S)-allantoin + H2O = allantoate.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1.
Subunit structure	Homotetramer By similarity.
Post-translational modification	Carbamylation allows a single lysine to coordinate two zinc ions By similarity.
Sequence similarities	Belongs to the DHOase family. Allantoinase subfamily.

Ontologies

Keywords
Biological process	Purine metabolism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	allantoin catabolic process Inferred from electronic annotation. Source: InterPro purine base metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	allantoinase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 510	510	Probable allantoinase 2		PRO_0000330751
Sites
	Metal binding	97	1	Zinc 1 By similarity
	Metal binding	99	1	Zinc 1 By similarity
	Metal binding	185	1	Zinc 1; via carbamate group By similarity
	Metal binding	185	1	Zinc 2; via carbamate group By similarity
	Metal binding	228	1	Zinc 2 By similarity
	Metal binding	287	1	Zinc 2 By similarity
	Metal binding	360	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	185	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55C91-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: AEA0E212B455B617	FASTA	510	57,323
	10 20 30 40 50 60 MEIWKVIFSI WFLLFQNFVL SAKNDDNKLK VIRGRNVIYN GNVIPLSILI RNGKTIGIKD 70 80 90 100 110 120 YSFNPKKLNE NYEILYDDRE CNNNEDFIIM GGLVDSHVHV NEPGRTEWEG FESATSAAAA 130 140 150 160 170 180 GGVTTIVDMP LNSSPVTTSF KNLLDKIESM KGKLRVDVGL LGGIVPGNSK EIKKMVLQGG 190 200 210 220 230 240 VLGFKSFLLP SGIDEFPPVN ENDIQEAMNE MKLLKCQYNN SDVIMMFHAE VEEPIKEATV 250 260 270 280 290 300 RLKNENADPK LYKTYLDSRP KISENQAISK LIDITRQNQI VSTHIVHLSS SESIEQIREA 310 320 330 340 350 360 MDQGVPISAE TTYNYLHLTS ESVPYGNTLF KSAPPVREHE NKELLWNAII NGTIKLIVSD 370 380 390 400 410 420 HSPCTINLKQ LKEDNQSIGD FLKAWGGISS LELGLPIIWT ECKNRGIPIT QLSEWLSNGP 430 440 450 460 470 480 SKLVGLNDRK GSIEIGRDAD FVIFNPNESF IVNEKKLFLK NKFSAYNGEK LFGVVYETIL 490 500 510 RGNSIFKKGD NKIKKIIGQR LIKSNLINKK

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000005 Genomic DNA. Translation: EAL72431.1.
RefSeq	XP_646590.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q55C91.
Genome annotation databases
GeneID	3397461.
GenomeReviews	Gene locus allB2 in contig CM000150_GR.
KEGG	ddi:DDB_0231351.
Organism-specific databases
dictyBase	DDB_G0270162. allB2.
Phylogenomic databases
OMA	TCFHYLC.
Family and domain databases
InterPro	IPR017593. Allantoinase. IPR006680. Amidohydro_1. IPR002195. Dihydroorotase_CS. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
TIGRFAMs	TIGR03178. allantoinase. 1 hit.
PROSITE	PS00482. DIHYDROOROTASE_1. 1 hit. PS00483. DIHYDROOROTASE_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALN2_DICDI

Accession

Primary (citable) accession number: Q55C91

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	May 24, 2005
Last modified:	November 3, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)